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P46821

- MAP1B_HUMAN

UniProt

P46821 - MAP1B_HUMAN

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Protein
Microtubule-associated protein 1B
Gene
MAP1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Facilitates tyrosination of alpha-tubulin in neuronal microtubules By similarity. Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing.1 Publication

GO - Molecular functioni

  1. hydrolase activity Source: InterPro
  2. protein binding Source: UniProtKB
  3. structural molecule activity Source: ProtInc

GO - Biological processi

  1. axon extension Source: Ensembl
  2. cellular process Source: DFLAT
  3. dendrite development Source: Ensembl
  4. establishment of monopolar cell polarity Source: Ensembl
  5. microtubule bundle formation Source: Ensembl
  6. mitochondrion transport along microtubule Source: Ensembl
  7. negative regulation of intracellular transport Source: Ensembl
  8. positive regulation of axon extension Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Cleaved into the following 2 chains:
Gene namesi
Name:MAP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6836. MAP1B.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasm. Cell junctionsynapse By similarity. Cell projectiondendritic spine By similarity
Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers By similarity.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: HPA
  3. cytosol Source: Ensembl
  4. dendritic spine Source: UniProtKB-SubCell
  5. microtubule Source: UniProtKB-KW
  6. microtubule associated complex Source: ProtInc
  7. plasma membrane Source: DFLAT
  8. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 24682467Microtubule-associated protein 1B
PRO_0000018604Add
BLAST
Chaini2 – 22062205MAP1B heavy chain
PRO_0000418379Add
BLAST
Chaini2207 – 2468262MAP1 light chain LC1
PRO_0000018605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei541 – 5411Phosphoserine By similarity
Modified residuei544 – 5441Phosphoserine By similarity
Modified residuei561 – 5611Phosphoserine By similarity
Modified residuei614 – 6141Phosphoserine By similarity
Modified residuei828 – 8281Phosphoserine1 Publication
Modified residuei831 – 8311Phosphoserine2 Publications
Modified residuei832 – 8321Phosphoserine2 Publications
Modified residuei937 – 9371Phosphoserine1 Publication
Modified residuei992 – 9921Phosphoserine2 Publications
Modified residuei995 – 9951Phosphoserine2 Publications
Modified residuei1016 – 10161Phosphoserine3 Publications
Modified residuei1144 – 11441Phosphoserine1 Publication
Modified residuei1154 – 11541Phosphoserine1 Publication
Modified residuei1156 – 11561Phosphoserine1 Publication
Modified residuei1208 – 12081Phosphoserine1 Publication
Modified residuei1252 – 12521Phosphoserine1 Publication
Modified residuei1256 – 12561Phosphoserine1 Publication
Modified residuei1260 – 12601Phosphoserine1 Publication
Modified residuei1265 – 12651Phosphoserine2 Publications
Modified residuei1276 – 12761Phosphoserine1 Publication
Modified residuei1280 – 12801Phosphoserine1 Publication
Modified residuei1282 – 12821Phosphothreonine2 Publications
Modified residuei1312 – 13121Phosphoserine By similarity
Modified residuei1378 – 13781Phosphoserine1 Publication
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1389 – 13891Phosphoserine1 Publication
Modified residuei1396 – 13961Phosphoserine2 Publications
Modified residuei1400 – 14001Phosphoserine3 Publications
Modified residuei1427 – 14271Phosphoserine3 Publications
Modified residuei1438 – 14381Phosphoserine2 Publications
Modified residuei1443 – 14431Phosphoserine2 Publications
Modified residuei1501 – 15011Phosphoserine2 Publications
Modified residuei1618 – 16181Phosphoserine1 Publication
Modified residuei1620 – 16201Phosphoserine1 Publication
Modified residuei1625 – 16251Phosphoserine1 Publication
Modified residuei1653 – 16531Phosphoserine1 Publication
Modified residuei1779 – 17791Phosphoserine3 Publications
Modified residuei1782 – 17821Phosphoserine2 Publications
Modified residuei1785 – 17851Phosphoserine1 Publication
Modified residuei1788 – 17881Phosphothreonine2 Publications
Modified residuei1797 – 17971Phosphoserine1 Publication
Modified residuei1915 – 19151Phosphoserine1 Publication
Modified residuei1917 – 19171Phosphoserine1 Publication
Modified residuei1965 – 19651Phosphoserine1 Publication
Modified residuei2271 – 22711Phosphoserine1 Publication
Modified residuei2289 – 22891Phosphoserine1 Publication
Modified residuei2464 – 24641S-nitrosocysteine By similarity

Post-translational modificationi

LC1 is generated from MAP1B by proteolytic processing.
S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP46821.
PaxDbiP46821.
PRIDEiP46821.

PTM databases

PhosphoSiteiP46821.

Expressioni

Gene expression databases

ArrayExpressiP46821.
BgeeiP46821.
CleanExiHS_MAP1B.
GenevestigatoriP46821.

Organism-specific databases

HPAiCAB009792.
HPA022275.

Interactioni

Subunit structurei

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL By similarity. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1. Interacts with TMEM185A. Interacts with MAP1LC3B.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GANQ9H2C03EBI-764611,EBI-764342
TP53P046376EBI-764611,EBI-366083

Protein-protein interaction databases

BioGridi110304. 41 interactions.
DIPiDIP-33474N.
IntActiP46821. 27 interactions.
MINTiMINT-243072.
STRINGi9606.ENSP00000296755.

Structurei

3D structure databases

ProteinModelPortaliP46821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1878 – 189417MAP1B 1
Add
BLAST
Repeati1895 – 191117MAP1B 2
Add
BLAST
Repeati1912 – 192817MAP1B 3
Add
BLAST
Repeati1929 – 194517MAP1B 4
Add
BLAST
Repeati1946 – 196217MAP1B 5
Add
BLAST
Repeati1963 – 197917MAP1B 6
Add
BLAST
Repeati1997 – 201317MAP1B 7
Add
BLAST
Repeati2014 – 203017MAP1B 8
Add
BLAST
Repeati2031 – 204717MAP1B 9
Add
BLAST
Repeati2048 – 206417MAP1B 10
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2294 – 2468175Mediates interaction with TMEM185A
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi589 – 790202Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)
Add
BLAST

Domaini

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.

Sequence similaritiesi

Belongs to the MAP1 family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP46821.
KOiK10429.
OMAiRTPVQDH.
OrthoDBiEOG773XKP.
PhylomeDBiP46821.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamiPF00414. MAP1B_neuraxin. 5 hits.
[Graphical view]
PROSITEiPS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46821-1 [UniParc]FASTAAdd to Basket

« Hide

MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE     50
HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL 100
HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL 150
ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN 200
LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT 250
SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 300
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI 350
SPDLGVVFLN VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR 400
SVGNTIDPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE 450
FILPNGQEVD LPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE 500
GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD SRESLKPAAK 550
PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 600
SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK 650
EEKEKPKKEV AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV 700
KKETPPKEVK KEVKKEEKKE VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK 750
KPAALKPKVP KKEESVKKDS VAAGKPKEKG KIKVIKKEGK AAEAVAAAVG 800
TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF EELKAEEVDV 850
TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 900
GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE 950
AEEPEEDGEE HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA 1000
EEDMDEAIEK GEAEQSEEEA DEEDKAEDAR EEEYEPEKME AEDYVMAVVD 1050
KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE PASSIHDETL PGGSESEATA 1100
SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR DVMSDETNNE 1150
ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 1200
NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK 1250
VSPSKSPSLS PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE 1300
VTQEVVEEHC ASPEDKTLEV VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT 1350
EVIEKPPAVP VSFEFSDAKD ENERASVSPM DEPVPDSESP IEKVLSPLRS 1400
PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD QVSPVSEMTS 1450
TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 1500
SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA 1550
SVSTASVATS SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT 1600
FQETEMSPSK EECPRPMSIS PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG 1650
QESPEQSLAM DFSRQSPDHP TVGAGVLHIT ENGPTEVDYS PSDMQDSSLS 1700
HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ IASPLQEDTL 1750
SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 1800
SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD 1850
LSTPGLEKDS GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD 1900
VGGYYYEKIE RTTKSPSDSG YSYETIGKTT KTPEDGDYSY EIIEKTTRTP 1950
EEGGYSYDIS EKTTSPPEVS GYSYEKTERS RRLLDDISNG YDDSEDGGHT 2000
LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY CYETAEKITR 2050
TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 2100
FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV 2150
SESAPSQTDS DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP 2200
PPAPVQDRSP SPRHPDVSMV DPEALAIEQN LGKALKKDLK EKTKTKKPGT 2250
KTKSSSPVKK SDGKSKPLAA SPKPAGLKES SDKVSRVASP KKKESVEKAA 2300
KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG TTKTTKSSAV 2350
PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 2400
VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS 2450
SSTVVMQDES FPACKIEL 2468
Length:2,468
Mass (Da):270,634
Last modified:January 11, 2011 - v2
Checksum:i3FFDCB2E20049A8A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036016
Natural varianti574 – 5741V → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036017
Natural varianti594 – 5941I → V.3 Publications
Corresponds to variant rs1866374 [ dbSNP | Ensembl ].
VAR_024530
Natural varianti869 – 8691E → G.
Corresponds to variant rs16876070 [ dbSNP | Ensembl ].
VAR_030347
Natural varianti1296 – 12961P → L.
Corresponds to variant rs34093016 [ dbSNP | Ensembl ].
VAR_034105
Natural varianti1917 – 19171S → R.
Corresponds to variant rs13153166 [ dbSNP | Ensembl ].
VAR_056123

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06237 mRNA. Translation: AAA18904.1.
BN001084 mRNA. Translation: CAM06633.1.
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1.
CCDSiCCDS4012.1.
RefSeqiNP_005900.2. NM_005909.3.
UniGeneiHs.335079.

Genome annotation databases

EnsembliENST00000296755; ENSP00000296755; ENSG00000131711.
GeneIDi4131.
KEGGihsa:4131.
UCSCiuc003kbw.4. human.

Polymorphism databases

DMDMi317373388.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L06237 mRNA. Translation: AAA18904.1 .
BN001084 mRNA. Translation: CAM06633.1 .
AC012609 Genomic DNA. No translation available.
AC093218 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95697.1 .
CCDSi CCDS4012.1.
RefSeqi NP_005900.2. NM_005909.3.
UniGenei Hs.335079.

3D structure databases

ProteinModelPortali P46821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110304. 41 interactions.
DIPi DIP-33474N.
IntActi P46821. 27 interactions.
MINTi MINT-243072.
STRINGi 9606.ENSP00000296755.

PTM databases

PhosphoSitei P46821.

Polymorphism databases

DMDMi 317373388.

Proteomic databases

MaxQBi P46821.
PaxDbi P46821.
PRIDEi P46821.

Protocols and materials databases

DNASUi 4131.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296755 ; ENSP00000296755 ; ENSG00000131711 .
GeneIDi 4131.
KEGGi hsa:4131.
UCSCi uc003kbw.4. human.

Organism-specific databases

CTDi 4131.
GeneCardsi GC05P071438.
HGNCi HGNC:6836. MAP1B.
HPAi CAB009792.
HPA022275.
MIMi 157129. gene.
neXtProti NX_P46821.
PharmGKBi PA30581.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000063256.
HOVERGENi HBG052409.
InParanoidi P46821.
KOi K10429.
OMAi RTPVQDH.
OrthoDBi EOG773XKP.
PhylomeDBi P46821.
TreeFami TF350229.

Miscellaneous databases

ChiTaRSi MAP1B. human.
GeneWikii MAP1B.
GenomeRNAii 4131.
NextBioi 16218.
PROi P46821.
SOURCEi Search...

Gene expression databases

ArrayExpressi P46821.
Bgeei P46821.
CleanExi HS_MAP1B.
Genevestigatori P46821.

Family and domain databases

Gene3Di 3.60.15.10. 2 hits.
InterProi IPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view ]
PANTHERi PTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
Pfami PF00414. MAP1B_neuraxin. 5 hits.
[Graphical view ]
PROSITEi PS00230. MAP1B_NEURAXIN. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15."
    Lien L.L., Feener C., Fischbach N., Kunkel L.M.
    Genomics 22:273-280(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
    Tissue: Fetal brain.
  2. "Hmob3 brain-specific sequence is a part of phylogenetically conserved human MAP1B gene 3'-untranslated region."
    Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A.
    Biomol. Eng. 20:91-96(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-594.
  5. Bienvenut W.V., Pchelintsev N., Adams P.D.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070; 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung fibroblast.
  6. Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin."
    Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y.
    J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  8. "Cloning of a novel neuronally expressed orphan G-protein-coupled receptor which is up-regulated by erythropoietin, interacts with microtubule-associated protein 1b and colocalizes with the 5-hydroxytryptamine 2a receptor."
    Maurer M.H., Gruenewald S., Gassler N., Rossner M., Propst F., Wuerz R., Weber D., Kuner T., Kuschinsky W., Schneider A.
    J. Neurochem. 91:1007-1017(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM185A.
  9. "Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival."
    Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y.
    Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016; SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427; SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND THR-1788, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
    Zou B., Yan H., Kawasaki F., Ordway R.W.
    Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE SITE.
  14. "DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing."
    Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R.
    J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396; SER-1400 AND SER-1501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995; SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256; SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400; SER-1427; SER-1438; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785; THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
    Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
    Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1LC3B.
  24. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.

Entry informationi

Entry nameiMAP1B_HUMAN
AccessioniPrimary (citable) accession number: P46821
Secondary accession number(s): A2BDK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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